Reviewed, UniProtKB/Swiss-Prot O87864 (KATG_STRRE)

Names and origin

Protein names

Recommended name:
    Catalase-peroxidase
      Short name=CP
    EC=1.11.1.6
    EC=1.11.1.7
Alternative name(s):
    Peroxidase/catalase

Gene names

Name:	katG
Synonyms:	cpeB

Organism

Streptomyces reticuli

Taxonomic identifier

1926 [NCBI]

Taxonomic lineage

Bacteria › Actinobacteria › Actinobacteridae › Actinomycetales › Streptomycineae › Streptomycetaceae › Streptomyces

Protein attributes

Sequence length	740 AA.
Sequence status	Complete.
Sequence processing	The displayed sequence is not processed.
Protein existence	Evidence at protein level.

General annotation (Comments)

Function	Bifunctional enzyme with both catalase and broad-spectrum peroxidase activity. Ref.1
Catalytic activity	2 H2O2 = O2 + 2 H2O. HAMAP MF_01961 Donor + H2O2 = oxidized donor + 2 H2O. HAMAP MF_01961
Cofactor	Binds 1 heme B (iron-protoporphyrin IX) group per dimer. Ref.1
Subunit structure	Homodimer. Ref.1
Post-translational modification	The covalent Trp-Tyr-Met adduct is important for the catalase, but not the peroxidase activity of the enzyme By similarity.
Sequence similarities	Belongs to the peroxidase family. Peroxidase/catalase subfamily.

Ontologies

Keywords
Biological process	Hydrogen peroxide
Ligand	Heme Iron Metal-binding
Molecular function	Oxidoreductase Peroxidase
Technical term	Direct protein sequencing
Gene Ontology (GO)
Biological process	hydrogen peroxide catabolic process Inferred from electronic annotation. Source: UniProtKB-KW oxidation reduction Inferred from electronic annotation. Source: UniProtKB-KW
Molecular function	catalase activity Inferred from electronic annotation. Source: HAMAP heme binding Inferred from electronic annotation. Source: InterPro
Complete GO annotation...

Sequence annotation (Features)

	Feature key	Position(s)	Length	Description	Graphical view	Feature identifier
Molecule processing
	Chain	1 – 740	740	Catalase-peroxidase HAMAP MF_01961		PRO_0000055577
Sites
	Active site	109	1	Proton acceptor By similarity
	Metal binding	272	1	Iron (heme axial ligand) By similarity
	Site	105	1	Transition state stabilizer By similarity
Amino acid modifications
	Cross-link	108 ↔ 231		Tryptophyl-tyrosyl-methioninium (Trp-Tyr) (with M-257) By similarity
	Cross-link	231 ↔ 257		Tryptophyl-tyrosyl-methioninium (Tyr-Met) (with W-108) By similarity

Sequences

	Sequence		Length	Mass (Da)
	O87864-1 [UniParc]. Last modified November 1, 1998. Version 1. Checksum: E21860AFE4B4A40E	FASTA	740	81,346
	10 20 30 40 50 60 MTENHDAIVT DAKSEGSGGC PVAHDRALHP TQGGGNRQWW PERLNLKILA KNPAVANPLD 70 80 90 100 110 120 EDFDYAEAFK ALDLAAVKRD IAEVLTTSQD WWPADFGNYG PLMIRMAWHS AGTYRISDGR 130 140 150 160 170 180 GGAGAGQQRF APLNSWPDNG NLDKARRLLW PVKKKYGQSI SWADLLILTG NVALETMGFK 190 200 210 220 230 240 TFGFGGGRAD VWEAEEDVYW GPETTWLDDR RYTGDRELEN PLGAVQMGLI YVNPEGPNGN 250 260 270 280 290 300 PDPIAAARDI RETFRRMAMN DEETVALIAG GHTFGKTHGA GPADHVGADP EAASLEEQGL 310 320 330 340 350 360 GWRSTYGTGK GADAITSGLE VTWTSTPTQW SNGFFKNLFE YEYELEQSPA GAHQWVAKNA 370 380 390 400 410 420 PEIIPDAHDP SKKHRPRMLT TDLSLRFDPI YEPISRRFYE NPEEFADAFA RAWYKLTHRD 430 440 450 460 470 480 MGPKSLYLGP EVPEETLLWQ DPLPEREGEL IDDADIAILK TKLLESGLSV SQLVTTAWAS 490 500 510 520 530 540 ASTFRASDKR GGANGARIRL APQRGWEVND PDQLAQVLRT LENVQQEFNA SSGAKKVSLA 550 560 570 580 590 600 DLIVLGGAAG VEKAAKEAGF EIQVPFTPGR VDATEEHTDV ESFEALEPTA DGFRNYLGKG 610 620 630 640 650 660 NRLPAEYLLL DKANLLNLSA PEMTVLVGGL RVLGANHQQS QLGVFTKTPG VLTNDFFVNL 670 680 690 700 710 720 LDMGTTWKAT SEDQTTFEGR DAATGEVKWA GSRADLVFGS NSELRALAEV YASDDAKEKF 730 740 VKDFVAAWHK VMDADRFDLV

References

[1]

"The mycelium-associated Streptomyces reticuli catalase-peroxidase, its gene and regulation by FurS." Zou P., Borovok I., Ortiz de Orue Lucana D., Muller D., Schrempf H. Microbiology 145:549-559(1999) [PubMed: 10217488] [Abstract] Cited for: NUCLEOTIDE SEQUENCE [GENOMIC DNA], PARTIAL PROTEIN SEQUENCE, FUNCTION, SUBUNIT, HEME-BINDING. Strain: Tu45.

Cross-references

Sequence databases
EMBLGenBankDDBJ	Y14317 Genomic DNA. Translation: CAA74698.1.
3D structure databases
HSSP	HSSP built from PDB template 1MWV based on UniProtKB Q939D2.
ModBase	Search...
Protein family/group databases
PeroxiBase	2330. SretCP01.
Enzyme and pathway databases
BRENDA	1.11.1.6. 257915.
Family and domain databases
HAMAP	MF_01961. [Tree]
InterPro	IPR000763. Catalase_proxase. IPR002016. Haem_peroxidase_pln/fun/bac. IPR019794. Peroxidases_AS. IPR019793. Peroxidases_heam-ligand_BS. [Graphical view]
Pfam	PF00141. peroxidase. 2 hits. [Graphical view]
PRINTS	PR00460. BPEROXIDASE. PR00458. PEROXIDASE.
TIGRFAMs	TIGR00198. cat_per_HPI. 1 hit.
PROSITE	PS00435. PEROXIDASE_1. 1 hit. PS00436. PEROXIDASE_2. 1 hit. PS50873. PEROXIDASE_4. 1 hit. [Graphical view]
ProtoNet	Search...

Entry information

Entry name

KATG_STRRE

Accession

Primary (citable) accession number: O87864

Entry history

Integrated into UniProtKB/Swiss-Prot:	December 1, 2000
Last sequence update:	November 1, 1998
Last modified:	May 5, 2009
This is version 55 of the entry and version 1 of the sequence. [Complete history]

Entry status

Reviewed (UniProtKB/Swiss-Prot)

Annotation project

HAMAP (High-quality Automated and Manual Annotation of microbial Proteomes)